Inhibition of MMP2-PEX by a novel ester of dihydroxy cinnamic and linoleic acid from the seagrass Cymodocea serrulata.

ABSTRACT: Matrix metalloproteinases (MMPs) are pivotal for cancer cell migration and metastasis which are generally over-expressed in such cell types. Many drugs targeting MMPs do so by binding to the conserved catalytic domains and thus exhibit poor selectivity due to domain-similarities with other proteases. We report herein the binding of a novel compound [3-(E-3,4-dihydroxycinnamaoyloxyl)-2-hydroxypropyl 9Z, 12Z-octadeca-9, 12-dienoate; Mol. wt: 516.67 Da], (C₁), isolated from a seagrass, Cymodocea serrulata to the unconserved hemopexin-like (PEX) domain of MMP2 (- 9.258 kcal/mol). MD simulations for 25 ns, suggest stable ligand-target binding. In addition, C₁ killed an ovarian cancer cell line, PA1 at IC₅₀: 5.8 μM (lesser than Doxorubicin: 8.6 µM) and formed mic

SUBMITTER: Christina VS 

PROVIDER: S-EPMC8169913 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature